Domain-specific folding of the tandem β-propeller protein Coronin 7 (Coro7) by CCT/TRiC DOI Creative Commons
DeHaven J. McCrary, Teri Naismith, Silvia Jansen

et al.

bioRxiv (Cold Spring Harbor Laboratory), Journal Year: 2025, Volume and Issue: unknown

Published: March 11, 2025

ABSTRACT The Chaperonin containing tailless complex polypeptide 1 (CCT) or TCP-1 ring (TRiC) plays a central role in maintaining cellular homeostasis by supporting protein folding and damping aggregation. Besides the abundant cytoskeletal proteins, actin tubulin, CCT/TRiC is emerging as an obligate chaperone for WD40 which are comprised of one multiple β-propeller domains. To date, only proteins consisting single domain have been described substrates. Using combination biotin proximity ligation, mass spec analysis co-immunoprecipitation, we here identify tandem protein, Coronin 7 (Coro7), novel interactor. Transient knockdown further severely diminished expression Coro7, suggesting that Coro7 bona fide substrate. Interestingly, co-immunoprecipitation truncated demonstrated interacts with first Coro7. In line this, fusion miniTurboID tag to N- C-terminus showed significant enrichment all subunits first, but not second domain. Similarly, individual domains generated introduction protease cleavage site full length confirmed binds Altogether, our study shows can also function multi-β-propeller likely initiating domain, then help template autonomous consecutive

Language: Английский

The role of molecular chaperone CCT/TRiC in translation elongation: A literature review DOI Creative Commons

Yueyue Que,

Yudan Qiu,

Zheyu Ding

et al.

Heliyon, Journal Year: 2024, Volume and Issue: 10(7), P. e29029 - e29029

Published: April 1, 2024

Protein synthesis from mRNA is an energy-intensive and strictly controlled biological process. Translation elongation a well-coordinated multifactorial step in translation that ensures the accurate efficient addition of amino acids to growing nascent-peptide chain encoded sequence messenger RNA (mRNA). Which undergoes dynamic regulation due cellular state environmental determinants. An expanding body research points translational as crucial process controls through multiple feedback mechanisms. Molecular chaperones are key players protein homeostasis keep balance between synthesis, folding, assembly, degradation. Chaperonin-containing tailless complex polypeptide 1 (CCT) or ring (TRiC) essential eukaryotic molecular chaperone plays role assisting folding suppressing aggregation. In this review, we give overview factors influence elongation, focusing on different functions including how they affect rates post-translational modifications. We also provide understanding mechanisms by which CCT roles phase synthesis.

Language: Английский

Citations

6
Revisiting the chaperonin T‐complex protein‐1 ring complex in human health and disease: A proteostasis modulator and beyond DOI

Chenglong Zeng,

Shenqi Han, Yonglong Pan

et al.

Clinical and Translational Medicine, Journal Year: 2024, Volume and Issue: 14(2)

Published: Feb. 1, 2024

Language: Английский

Citations

5
HSP70 is a chaperone for IL-33 secretion and function in chronic airway disease DOI Open Access
Omar A. Osorio, Colin E. Kluender,

Heather E. Raphael

et al.

bioRxiv (Cold Spring Harbor Laboratory), Journal Year: 2025, Volume and Issue: unknown

Published: Feb. 5, 2025

ABSTRACT Rationale IL-33 is a key driver of type 2 inflammation relevant to airway epithelial biology. However, the mechanisms for secretion and regulation in context chronic disease poorly understood. Objectives We sought define how associated isoform Δ34 that escapes nuclear sequestration tonically secreted from cells can be recruited non-canonical secretory pathways. Methods interaction with HSP70 was assessed validated by affinity purification, mass-spectrometry miniTurboID proximity labeling. Secretion activity reporter assays were used probe effect on receptor binding. Human biospecimens analyzed dysregulation heat shock pathways revealing modulation TCP1 complex intermediates. Measurements Main Results confirmed interacts directly , recruits cytokine vesicular compartment enhances stability upon secretion. IL-33, other mediators proteostasis found dysregulated extracellular vesicles. The interactome characterized novel modulators identified. Conclusions This study confirms role function may amenable therapeutic targeting diseases.

Language: Английский

Citations

0
A nuclear TRiC/CCT chaperonin assembles meiotic HORMAD proteins into chromosome axes competent for crossing over DOI Creative Commons
Monique Zetka,

Abdul Mohammad Pezeshki,

Steven J.M. Jones

et al.

Published: March 3, 2025

Abstract The meiotic chromosome axis organizes chromatin and sets the stage for homolog pairing recombination. M eiotic HORMA d omain proteins (mHORMADs) are conserved components that conformationally transform during target binding. In C. elegans, four functionally distinct mHORMADs directly interact, but how binding between them is restricted to assembly unknown. Using a mutation in delays assembly, we isolated suppressor TRiC/CCT chaperonin subunit restored mHORMAD localization. CCT-4 associates with forms vivo complexes mHORMADs, while germline disruption of TRiC results defects, indicating nuclear function alongside chromosomes. We propose chromosome-tethered folds into active local population required morphogenesis. More broadly, our support model spatially-restricted folding by mechanism controlling multimeric tightly co-ordinated events.

Language: Английский

Citations

0
Domain-specific folding of the tandem β-propeller protein Coronin 7 (Coro7) by CCT/TRiC DOI Creative Commons
DeHaven J. McCrary, Teri Naismith, Silvia Jansen

et al.

bioRxiv (Cold Spring Harbor Laboratory), Journal Year: 2025, Volume and Issue: unknown

Published: March 11, 2025

ABSTRACT The Chaperonin containing tailless complex polypeptide 1 (CCT) or TCP-1 ring (TRiC) plays a central role in maintaining cellular homeostasis by supporting protein folding and damping aggregation. Besides the abundant cytoskeletal proteins, actin tubulin, CCT/TRiC is emerging as an obligate chaperone for WD40 which are comprised of one multiple β-propeller domains. To date, only proteins consisting single domain have been described substrates. Using combination biotin proximity ligation, mass spec analysis co-immunoprecipitation, we here identify tandem protein, Coronin 7 (Coro7), novel interactor. Transient knockdown further severely diminished expression Coro7, suggesting that Coro7 bona fide substrate. Interestingly, co-immunoprecipitation truncated demonstrated interacts with first Coro7. In line this, fusion miniTurboID tag to N- C-terminus showed significant enrichment all subunits first, but not second domain. Similarly, individual domains generated introduction protease cleavage site full length confirmed binds Altogether, our study shows can also function multi-β-propeller likely initiating domain, then help template autonomous consecutive

Language: Английский

Citations

0